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Reviewed, UniProtKB/Swiss-Prot Q7VQL0 (SYI_BLOFL)

Last modified February 9, 2010. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Isoleucyl-tRNA synthetase
    EC=6.1.1.5
Alternative name(s):
    Isoleucine--tRNA ligase
      Short name=IleRS
Gene names
Name: ileS
Ordered Locus Names: Bfl118
OrganismBlochmannia floridanus [Complete proteome] [HAMAP]
Taxonomic identifier203907 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeant endosymbiontsCandidatus Blochmannia

Protein attributes

Sequence length953 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) By similarity. HAMAP MF_02002

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP MF_02002

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_02002

Subunit structure

Monomer By similarity. HAMAP MF_02002

Subcellular location

Cytoplasm By similarity HAMAP MF_02002.

Domain

IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)) By similarity. HAMAP MF_02002

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processisoleucyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

isoleucine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 953953Isoleucyl-tRNA synthetase HAMAP MF_02002
PRO_0000098355

Regions

Motif58 – 6811"HIGH" region HAMAP MF_02002
Motif614 – 6185"KMSKS" region HAMAP MF_02002

Sites

Metal binding9161Zinc By similarity
Metal binding9191Zinc By similarity
Metal binding9361Zinc By similarity
Metal binding9391Zinc By similarity
Binding site5731Aminoacyl-adenylate By similarity
Binding site6171ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VQL0-1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: E4991E114C404932

FASTA953111,929
        10         20         30         40         50         60 
MADYKSTLNL PYTQFPMRGN LPIIEIKILE RWNRDNLYEI IRRKKNEKKL FLLHDGPPYA 

        70         80         90        100        110        120 
NGFIHLGHAV NKILKDIIIK FKGLSGYDAP YIPGWDCHGL PIELQVEKLI KKVNMDIDIN 

       130        140        150        160        170        180 
SQEFRNYCRE YVKKQIEIQK KDFIRLGILG EWKNPYLTMD YKTEANIIRT LGKIISNGYF 

       190        200        210        220        230        240 
YKGIKPVYWC FQCHSALANS EVEYNDYHYS NAVDVGFSIV ENVSINKIFN INCYIENIEL 

       250        260        270        280        290        300 
VIWTTTIWTL PANQAISIHP DYIYQLVKIL DNEKYLIIAA NLVNMFMNRI KCTMWQVLGE 

       310        320        330        340        350        360 
VLGSKLDRLT ARHPFMNFNV PLVLSKHIKL DSGTGLVHIA PDHGPDDYLI SKKYKFKNRD 

       370        380        390        400        410        420 
SLIDSNGYYL SNSHNRLCGL HIFNANEIII DLLYKSKNFL YFNANYQHSY PYCWRHKIPL 

       430        440        450        460        470        480 
IFRTTSQWFV NMDHNNLRDK LLRTLQQVRW IPDSGYSSMQ SMIVNRPDWC LSRQRVWGIP 

       490        500        510        520        530        540 
IPVFVHKKTE VLHPNTCIFI EQVAQLVEKY GIQIWWDLKN EDIILNKAES MNYQKIYDTL 

       550        560        570        580        590        600 
DVWFDSGSTH DSVILDRFNS KLKSKLQIDL YLEGVDQYRG WFMSSLIIAV AIKGYAPYKQ 

       610        620        630        640        650        660 
VLSHGFTIDD KGNKMSKSLG NIIRPLDIVN KFGSDILRLW VASSDYSKDM VISDDVLKNV 

       670        680        690        700        710        720 
TDIYRRIRNT IRFFLANIND FDPEKDLVQS NRMVALDQWA INHTLSVQVK IISNYEQYKF 

       730        740        750        760        770        780 
HNVIRYIMKF CSIEMGSFYL DVVKDRLYTL NKDSLARRSC QTALYHIIES MVRWIAPILS 

       790        800        810        820        830        840 
FTADEIWKYI PGNRSKYVFT EEWYDRLFKI DENQIVNSNY WNFFLNIRNK VNKVIEQERV 

       850        860        870        880        890        900 
NGIIKGSLEA DVILYVTPIL KKKLRILKNE LAFGLIVSSV MVLSIDDVDF NTIKENHEEN 

       910        920        930        940        950 
SDELKVVLKK SHGIKCLRCW NYTLSMSKNE NYLNICSRCV HNITGLGEDR RFF 

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References

[1]"The genome sequence of Blochmannia floridanus: comparative analysis of reduced genomes."
Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F., Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B., van Ham R.C.H.J., Gross R., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003) [PubMed: 12886019] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248583 Genomic DNA. Translation: CAD83639.1.
RefSeqNP_878425.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ7VQL0.

Genome annotation databases

GeneID1499318.
GenomeReviewsGene locus Bfl118 in contig BX248583_GR.
KEGGbfl:Bfl118.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHBG577712.
OMAKQVLTHG.
PhylomeDBQ7VQL0.

Enzyme and pathway databases

BioCycCBLO203907:BFL118-MONOMER.

Family and domain databases

HAMAPMF_02002. Ile_tRNA_synth_type1.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR010663. DNA_glyclase/IsotRNA_synth_Znf.
IPR002301. Ile-tRNA-synt_Ia.
IPR015905. Ile-tRNA-synt_Ia_N.
IPR018353. Isoleucyl-tRNA_synthetase.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_Ia_edit.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11946:SF9. Ile-tRNA-synt_Ia. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_BLOFL
AccessionPrimary (citable) accession number: Q7VQL0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2003
Last modified: February 9, 2010
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents